EC Number |
Protein Variants |
Reference |
---|
6.5.1.2 | A644I |
mutation in BRCT domain, comparable ligation activity with wild-type enzyme with nicked substrate in excess |
661092 |
6.5.1.2 | C408A |
inactive, unable to complement DNA-ligase-deficient yeast |
653376 |
6.5.1.2 | C411A |
inactive, unable to complement DNA-ligase-deficient yeast |
653376 |
6.5.1.2 | C412M |
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond |
1979 |
6.5.1.2 | C412T |
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond |
1979 |
6.5.1.2 | C412V |
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond |
1979 |
6.5.1.2 | C415A |
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond |
1979 |
6.5.1.2 | C415M |
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond |
1979 |
6.5.1.2 | C415T |
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond |
1979 |
6.5.1.2 | C415V |
Site-directed mutants: K118R, K118H, K118L, K118P1(CCC), K118P2(CCG), D120E, D120N, D120Y, D120G, D120A, D120V, K294R, K294Q, K294L1(CTG), K2942(CTC), K294P, K294P, R337K, R337Q, R337E, G339A, G339D, G339E, C412A, C412V, C412T, C412M, C415A, C415V, C415T, C415M, C428A, C428T, C433A, C433V, C433T and C433M. Studies show that residue K118 plays an essential role in the adenylation step, residue D120 may facilitate the deadenylation step, residue G339 and C433 may be involved in formation of the phosphodiester bond |
1979 |